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8OFN

Structure of the yellow fever virus (Asibi strain) dimeric envelope protein

Summary for 8OFN
Entry DOI10.2210/pdb8ofn/pdb
Related6EPK
DescriptorEnvelope glycoprotein, SULFATE ION (2 entities in total)
Functional Keywordsyellow fever envelope protein, asibi strain, viral protein
Biological sourceYellow fever virus
Total number of polymer chains2
Total formula weight93354.74
Authors
Covernton, E.,Vaney, M.C.,Barba-Spaeth, G.,Rey, F.A. (deposition date: 2023-03-16, release date: 2023-08-09, Last modification date: 2024-10-16)
Primary citationCrampon, E.,Covernton, E.,Vaney, M.C.,Dellarole, M.,Sommer, S.,Sharma, A.,Haouz, A.,England, P.,Lepault, J.,Duquerroy, S.,Rey, F.A.,Barba-Spaeth, G.
New insight into flavivirus maturation from structure/function studies of the yellow fever virus envelope protein complex.
Mbio, 14:e0070623-e0070623, 2023
Cited by
PubMed Abstract: All enveloped viruses enter cells by fusing their envelope with a target cell membrane while avoiding premature fusion with membranes of the producer cell-the latter being particularly important for viruses that bud at internal membranes. Flaviviruses bud in the endoplasmic reticulum, are transported through the TGN to reach the external milieu, and enter other cells via receptor-mediated endocytosis. The trigger for membrane fusion is the acidic environment of early endosomes, which has a similar pH to the TGN of the producer cell. The viral particles therefore become activated to react to mildly acidic pH only after their release into the neutral pH extracellular environment. Our study shows that for yellow fever virus (YFV), the mechanism of activation involves actively knocking out the fusion brake (protein pr) through a localized conformational change of the envelope protein upon exposure to the neutral pH external environment. Our study has important implications for understanding the molecular mechanism of flavivirus fusion activation in general and points to an alternative way of interfering with this process as an antiviral treatment.
PubMed: 37607061
DOI: 10.1128/mbio.00706-23
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.48 Å)
Structure validation

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